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Q27772

- C1TC_SPOFR

UniProt

Q27772 - C1TC_SPOFR

Protein

C-1-tetrahydrofolate synthase, cytoplasmic

Gene
N/A
Organism
Spodoptera frugiperda (Fall armyworm)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 3 (16 Jan 2004)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH.
    5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate.
    ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei195 – 1951NADPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi170 – 1723NADPBy similarity
    Nucleotide bindingi378 – 3858ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. formate-tetrahydrofolate ligase activity Source: UniProtKB-EC
    3. methenyltetrahydrofolate cyclohydrolase activity Source: UniProtKB-EC
    4. methylenetetrahydrofolate dehydrogenase (NADP+) activity Source: UniProtKB-EC

    GO - Biological processi

    1. folic acid-containing compound biosynthetic process Source: InterPro
    2. histidine biosynthetic process Source: UniProtKB-KW
    3. methionine biosynthetic process Source: UniProtKB-KW
    4. purine nucleotide biosynthetic process Source: UniProtKB-KW
    5. tetrahydrofolate interconversion Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Hydrolase, Ligase, Oxidoreductase

    Keywords - Biological processi

    Amino-acid biosynthesis, Histidine biosynthesis, Methionine biosynthesis, One-carbon metabolism, Purine biosynthesis

    Keywords - Ligandi

    ATP-binding, NADP, Nucleotide-binding

    Enzyme and pathway databases

    UniPathwayiUPA00193.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    C-1-tetrahydrofolate synthase, cytoplasmic
    Short name:
    C1-THF synthase
    Including the following 3 domains:
    Methylenetetrahydrofolate dehydrogenase (EC:1.5.1.5)
    Methenyltetrahydrofolate cyclohydrolase (EC:3.5.4.9)
    Formyltetrahydrofolate synthetase (EC:6.3.4.3)
    OrganismiSpodoptera frugiperda (Fall armyworm)
    Taxonomic identifieri7108 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaNoctuoideaNoctuidaeAmphipyrinaeSpodoptera

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 933933C-1-tetrahydrofolate synthase, cytoplasmicPRO_0000199325Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ27772.
    SMRiQ27772. Positions 10-294, 467-528.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 303303Methylenetetrahydrofolate dehydrogenase and cyclohydrolaseAdd
    BLAST
    Regioni51 – 555Substrate bindingBy similarity
    Regioni98 – 1003Substrate bindingBy similarity
    Regioni270 – 2745Substrate bindingBy similarity
    Regioni304 – 933630Formyltetrahydrofolate synthetaseAdd
    BLAST

    Domaini

    This trifunctional enzyme consists of two major domains: an N-terminal part containing the methylene-THF dehydrogenase and cyclohydrolase activities and a larger C-terminal part containing formyl-THF synthetase activity.

    Sequence similaritiesi

    In the N-terminal section; belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.Curated
    In the C-terminal section; belongs to the formate--tetrahydrofolate ligase family.Curated

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    3.40.50.720. 1 hit.
    HAMAPiMF_01543. FTHFS.
    MF_01576. THF_DHG_CYH.
    InterProiIPR000559. Formate_THF_ligase.
    IPR020628. Formate_THF_ligase_CS.
    IPR016040. NAD(P)-bd_dom.
    IPR027417. P-loop_NTPase.
    IPR000672. THF_DH/CycHdrlase.
    IPR020630. THF_DH/CycHdrlase_cat_dom.
    IPR020867. THF_DH/CycHdrlase_CS.
    IPR020631. THF_DH/CycHdrlase_NAD-bd_dom.
    [Graphical view]
    PfamiPF01268. FTHFS. 1 hit.
    PF00763. THF_DHG_CYH. 1 hit.
    PF02882. THF_DHG_CYH_C. 1 hit.
    [Graphical view]
    PRINTSiPR00085. THFDHDRGNASE.
    SUPFAMiSSF52540. SSF52540. 2 hits.
    PROSITEiPS00721. FTHFS_1. 1 hit.
    PS00722. FTHFS_2. 1 hit.
    PS00766. THF_DHG_CYH_1. 1 hit.
    PS00767. THF_DHG_CYH_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q27772-1 [UniParc]FASTAAdd to Basket

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    MWEPQGSLDP VLESIENELR DQVAEARSRW AGFDARLAIV QVGGREDSNV    50
    YIRMKLRAAE NIGITAEHIQ LPRDITETEL LANITSLNES PYVHGIIVQM 100
    PLDSVHPIDS HAITDAVSPD KDVDGLNTIN EGRVRVGDLS GFIPCTPAGC 150
    VELIKRTGVT IAGKNVVVLG RSRIVGTPVS ELLKWEHATV TVCHSKTKNL 200
    SEITKTADIL VVAIGRGEMV RGSWIKPGAV VIDCGINPIS DPTKKSGQRL 250
    VGDVAYEEAV QVASHVTPVP GGVGPMTVAM LMRNTVQAAR RQLDRLLAPT 300
    WPLRPLRITP LSPPPSDIVI ARSQKPKDIS ELAHEIGLFS NEVSQYGRTK 350
    AKISLSVLDR MRNQQGAKYI VVAGITPTPL GEGKSTTLLG LVQALSAHRG 400
    RNSFAVMRQP SQGPTFGVKG GAAGGGYSQV IPMEEFNLHL TGDIHAGTAA 450
    NNLLAAQMDA RIFHELTQKD GPLFDRLVPK IKGVRKFSPI QLRRLKRLGI 500
    TKTDPDTLTE GEKSKFARLN IDTSKIMWNR VVDLNDRYLR KITVGQSPTE 550
    KGFTRETAFD ISVASEIMAI LALGRDVEDI KERLANMVVA LDKSGNPVTA 600
    DDLGMTGALL VLLRDAFEPT LMQSLEGTPV LVHTGPFANI RHGCSSILAD 650
    KIAMKLAGEN GYVATEAGFG SDIGMEKFFD IKCRASGDTP HCAVIVSTVR 700
    ALKMHGGGPP VSAGMPLNDV YVQENLELLS KGLCNLGKHI SNGNKFGVPV 750
    VVAINKHGND TPAELNLVKE FAVKNGAFRA VLCDHWAKGG LGALELADAV 800
    IEACDSKSKF DFLYPLQLSI QEKIQIIAKE MYGAGQVEYT DEVLEKIKTF 850
    TDMGYDKFPI CMAKTSNSLT GDPAVKGAPT GFTLKINGIF ASVGAGFVVP 900
    MVGEISKMPG LPTRPSIYDI DLNTKTGEIE GLF 933
    Length:933
    Mass (Da):100,618
    Last modified:January 16, 2004 - v3
    Checksum:i55C3FA820C1A55CB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L36189 mRNA. Translation: AAA74302.1.
    PIRiS53523.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L36189 mRNA. Translation: AAA74302.1 .
    PIRi S53523.

    3D structure databases

    ProteinModelPortali Q27772.
    SMRi Q27772. Positions 10-294, 467-528.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00193 .

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    3.40.50.720. 1 hit.
    HAMAPi MF_01543. FTHFS.
    MF_01576. THF_DHG_CYH.
    InterProi IPR000559. Formate_THF_ligase.
    IPR020628. Formate_THF_ligase_CS.
    IPR016040. NAD(P)-bd_dom.
    IPR027417. P-loop_NTPase.
    IPR000672. THF_DH/CycHdrlase.
    IPR020630. THF_DH/CycHdrlase_cat_dom.
    IPR020867. THF_DH/CycHdrlase_CS.
    IPR020631. THF_DH/CycHdrlase_NAD-bd_dom.
    [Graphical view ]
    Pfami PF01268. FTHFS. 1 hit.
    PF00763. THF_DHG_CYH. 1 hit.
    PF02882. THF_DHG_CYH_C. 1 hit.
    [Graphical view ]
    PRINTSi PR00085. THFDHDRGNASE.
    SUPFAMi SSF52540. SSF52540. 2 hits.
    PROSITEi PS00721. FTHFS_1. 1 hit.
    PS00722. FTHFS_2. 1 hit.
    PS00766. THF_DHG_CYH_1. 1 hit.
    PS00767. THF_DHG_CYH_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure of a folate-dependent trifunctional enzyme from Spodoptera frugiperda."
      Tremblay G.B., MacKenzie R.E.
      Biochim. Biophys. Acta 1261:129-133(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Ovary.

    Entry informationi

    Entry nameiC1TC_SPOFR
    AccessioniPrimary (citable) accession number: Q27772
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 16, 2004
    Last sequence update: January 16, 2004
    Last modified: October 1, 2014
    This is version 82 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Multifunctional enzyme

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3